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Literature summary extracted from

  • Mehboob, S.; Guo, L.; Fu, W.; Mittal, A.; Yau, T.; Truong, K.; Johlfs, M.; Long, F.; Fung, L.; Johnson, M.
    Glutamate racemase dimerization inhibits dynamic conformational flexibility and reduces catalytic rates (2009), Biochemistry, 48, 7045-7055.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
5.1.1.3 drug development einzyme is potentially an attractive target for the development of new antibacterial agents because of being an essential enzyme Bacillus anthracis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.3 recombinant wild type and mutants are expressed in BL21(DE3) Escherichia coli cells Bacillus anthracis

Protein Variants

EC Number Protein Variants Comment Organism
5.1.1.3 K106A production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with an a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface Bacillus anthracis
5.1.1.3 K29A production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface Bacillus anthracis
5.1.1.3 P99A production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface Bacillus anthracis
5.1.1.3 Q86A production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with an at most 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface Bacillus anthracis
5.1.1.3 R214A production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface Bacillus anthracis
5.1.1.3 R214A/K106A production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface Bacillus anthracis
5.1.1.3 R25A production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface Bacillus anthracis
5.1.1.3 Y221A production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with an at most 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface Bacillus anthracis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.1.3 0.07
-
 D-glutamate recombinant wild type enzyme, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/mL diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.1
-
 D-glutamate mutant Q86A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.13
-
 D-glutamate mutant Y221A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.14
-
 D-glutamate mutant R25A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.16
-
 D-glutamate mutant R214A/K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.17
-
 D-glutamate mutant P99A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.25
-
 D-glutamate mutant K29A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.3
-
 D-glutamate mutant R214A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.42
-
 D-glutamate mutant K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 4.1
-
 L-glutamate mutant P99A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 5.8
-
 L-glutamate mutant R25A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 6.1
-
 L-glutamate recombinant RacE2 wild type enzyme, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 7.2
-
 L-glutamate mutant K29A, in 10 mM potassium phosphate (pH 8.2)and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 8.8
-
 L-glutamate mutant Q86A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 9.9
-
 L-glutamate mutant Y221A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 10.1
-
 L-glutamate mutant R214A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 10.8
-
 L-glutamate mutant K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 11
-
 L-glutamate mutant R214A/K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.1.3 L-glutamate Bacillus anthracis
-
 D-glutamate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.3 Bacillus anthracis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.3 by using nickel-nitrilotriacetic acid affinity chromatography and gel filtration Bacillus anthracis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.3 L-glutamate
-
 Bacillus anthracis D-glutamate
-
 r

Subunits

EC Number Subunits Comment Organism
5.1.1.3 dimer determined by gel filtration, RacE2 exist as a dimer in solution, but the monomeric enzyme is more active than the dimeric form Bacillus anthracis
5.1.1.3 monomer mutants R25A and K106A/R214A are completely monomeric at the concentration of 5 mg/ml Bacillus anthracis

Synonyms

EC Number Synonyms Comment Organism
5.1.1.3 glutamate racemase
-
 Bacillus anthracis
5.1.1.3 RACE
-
 Bacillus anthracis
5.1.1.3 RacE2
-
 Bacillus anthracis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.1.1.3 49
-
 Tm value (midpoint of thermal unfolding) of the wild type enzyme Bacillus anthracis
5.1.1.3 51
-
 Tm value (midpoint of thermal unfolding) of the R25A mutant Bacillus anthracis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.1.3 780
-
 D-glutamate recombinant wild type enzyme, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 2160
-
 D-glutamate mutant Q86A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 2760
-
 D-glutamate mutant Y221A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 5220
-
 D-glutamate mutant K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 6660
-
 D-glutamate mutant R214A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 7440
-
 D-glutamate mutant K29A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 7560
-
 D-glutamate mutant R25A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 7680
-
 D-glutamate mutant P99A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 7980
-
 D-glutamate mutant R214A/K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 116600
-
 L-glutamate recombinant wild type enzyme, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 144000
-
 L-glutamate mutant Q86A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 164400
-
 L-glutamate mutant P99A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 219600
-
 L-glutamate mutant K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 252000
-
 L-glutamate mutant Y221A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 278400
-
 L-glutamate mutant R214A/K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 294000
-
 L-glutamate mutant R25A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 306000
-
 L-glutamate mutant K29A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 355200
-
 L-glutamate mutant R214A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis

General Information

EC Number General Information Comment Organism
5.1.1.3 physiological function peptidoglycan synthesis Bacillus anthracis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.1.1.3 0.0031
-
 D-glutamate recombinant wild type enzyme, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.0035
-
 D-glutamate mutant K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.0045
-
 L-glutamate mutant Q86A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 0.0053
-
 L-glutamate recombinant wild type enzyme, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 0.0056
-
 L-glutamate mutant K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 0.0059
-
 D-glutamate mutant Y221A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.006
-
 D-glutamate mutant Q86A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.0062
-
 D-glutamate mutant R214A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.007
-
 L-glutamate mutant R214A/K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 0.0071
-
 L-glutamate mutant Y221A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 0.0083
-
 D-glutamate mutant K29A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.0098
-
 L-glutamate mutant R214A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 0.0111
-
 L-glutamate mutant P99A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 0.0118
-
 L-glutamate mutant K29A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 0.0125
-
 D-glutamate mutant P99A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.0139
-
 D-glutamate mutant R214A/K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis
5.1.1.3 0.014
-
 L-glutamate mutant R25A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol Bacillus anthracis
5.1.1.3 0.015
-
 D-glutamate mutant R25A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate Bacillus anthracis